1Q17
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
A | 0051287 | molecular_function | NAD binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
B | 0051287 | molecular_function | NAD binding |
B | 0070403 | molecular_function | NAD+ binding |
C | 0017136 | molecular_function | NAD-dependent histone deacetylase activity |
C | 0051287 | molecular_function | NAD binding |
C | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | CYS143 |
A | CYS146 |
A | CYS170 |
A | CYS173 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | CYS143 |
B | CYS146 |
B | CYS170 |
B | CYS173 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 401 |
Chain | Residue |
C | CYS146 |
C | CYS170 |
C | CYS173 |
C | CYS143 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 701 |
Chain | Residue |
C | ARG204 |
C | ARG240 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 702 |
Chain | Residue |
B | TRP202 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 703 |
Chain | Residue |
A | ARG204 |
A | ARG240 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 704 |
Chain | Residue |
B | ARG204 |
B | ARG240 |
site_id | AC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE APR A 1001 |
Chain | Residue |
A | GLY32 |
A | ALA33 |
A | GLY34 |
A | THR37 |
A | ASP43 |
A | PHE44 |
A | ARG45 |
A | TYR52 |
A | GLN115 |
A | HIS135 |
A | GLY223 |
A | THR224 |
A | SER225 |
A | VAL228 |
A | ASN248 |
A | LEU249 |
A | GLU250 |
A | GLN268 |
A | TYR269 |
A | SER270 |
A | HOH1003 |
A | HOH1025 |
A | HOH1041 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE APR B 1002 |
Chain | Residue |
B | GLY32 |
B | ALA33 |
B | GLY34 |
B | THR37 |
B | ASP43 |
B | PHE44 |
B | ARG45 |
B | TYR52 |
B | GLN115 |
B | HIS135 |
B | GLY223 |
B | THR224 |
B | SER225 |
B | VAL228 |
B | ASN248 |
B | LEU249 |
B | GLN268 |
B | TYR269 |
B | SER270 |
B | HOH1007 |
B | HOH1009 |
B | HOH1023 |
B | HOH1024 |
B | HOH1046 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE APR C 1003 |
Chain | Residue |
C | GLY32 |
C | ALA33 |
C | GLY34 |
C | THR37 |
C | ASP43 |
C | PHE44 |
C | ARG45 |
C | TYR52 |
C | GLN115 |
C | HIS135 |
C | GLY223 |
C | THR224 |
C | SER225 |
C | VAL228 |
C | ASN248 |
C | LEU249 |
C | GLN268 |
C | TYR269 |
C | SER270 |
C | HOH1022 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:20726530 |
Chain | Residue | Details |
A | HIS135 | |
B | HIS135 | |
C | HIS135 |
site_id | SWS_FT_FI2 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:15150415 |
Chain | Residue | Details |
A | GLY32 | |
B | SER270 | |
C | GLY32 | |
C | GLN115 | |
C | GLY223 | |
C | ASN248 | |
C | SER270 | |
A | GLN115 | |
A | GLY223 | |
A | ASN248 | |
A | SER270 | |
B | GLY32 | |
B | GLN115 | |
B | GLY223 | |
B | ASN248 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530, ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592 |
Chain | Residue | Details |
A | CYS143 | |
C | CYS146 | |
C | CYS170 | |
C | CYS173 | |
A | CYS146 | |
A | CYS170 | |
A | CYS173 | |
B | CYS143 | |
B | CYS146 | |
B | CYS170 | |
B | CYS173 | |
C | CYS143 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
C | SER2 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 240 |
Chain | Residue | Details |
A | PRO42 | hydrogen bond acceptor, steric role |
A | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
A | PHE44 | steric role, van der waals interaction |
A | ARG45 | electrostatic stabiliser, hydrogen bond donor |
A | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
A | ASP118 | activator, hydrogen bond acceptor |
A | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 240 |
Chain | Residue | Details |
B | PRO42 | hydrogen bond acceptor, steric role |
B | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
B | PHE44 | steric role, van der waals interaction |
B | ARG45 | electrostatic stabiliser, hydrogen bond donor |
B | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
B | ASP118 | activator, hydrogen bond acceptor |
B | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 240 |
Chain | Residue | Details |
C | PRO42 | hydrogen bond acceptor, steric role |
C | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
C | PHE44 | steric role, van der waals interaction |
C | ARG45 | electrostatic stabiliser, hydrogen bond donor |
C | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
C | ASP118 | activator, hydrogen bond acceptor |
C | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |